STXB1_RAT - dbPTM
STXB1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STXB1_RAT
UniProt AC P61765
Protein Name Syntaxin-binding protein 1
Gene Name Stxbp1
Organism Rattus norvegicus (Rat).
Sequence Length 594
Subcellular Localization Cytoplasm, cytosol . Membrane
Peripheral membrane protein.
Protein Description May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions..
Protein Sequence MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIGSTHILTPQKLLDTLKKLNKTDEEISS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
7Acetylation-MAPIGLKAVVGEKI
-CCCCCCHHHHCHHH
33.6422902405
13AcetylationLKAVVGEKIMHDVIK
CHHHHCHHHHHHHHH
39.1322902405
13UbiquitinationLKAVVGEKIMHDVIK
CHHHHCHHHHHHHHH
39.13-
20AcetylationKIMHDVIKKVKKKGE
HHHHHHHHHHHHCCC
51.9022902405
92AcetylationHSLISDFKDPPTAKY
HHHHHCCCCCCCCCC
74.4522902405
92UbiquitinationHSLISDFKDPPTAKY
HHHHHCCCCCCCCCC
74.45-
98AcetylationFKDPPTAKYRAAHVF
CCCCCCCCCEEEEEE
37.4322902405
110S-nitrosylationHVFFTDSCPDALFNE
EEEECCCCHHHHHHH
3.8322178444
110S-nitrosocysteineHVFFTDSCPDALFNE
EEEECCCCHHHHHHH
3.83-
120AcetylationALFNELVKSRAAKVI
HHHHHHHHHHHHHHH
47.01140591
120UbiquitinationALFNELVKSRAAKVI
HHHHHHHHHHHHHHH
47.01-
158PhosphorylationDSFQSFYSPHKAQMK
HHHHHHCCCCHHHCC
20.6530240740
184UbiquitinationATLCATLKEYPAVRY
HHHHHHHHHCCCCEE
51.34-
294UbiquitinationLWIALRHKHIAEVSQ
EEHHHHCHHHHHHCH
30.21-
294AcetylationLWIALRHKHIAEVSQ
EEHHHHCHHHHHHCH
30.2122902405
306PhosphorylationVSQEVTRSLKDFSSS
HCHHHHHHHHHCCCC
30.3316997485
308AcetylationQEVTRSLKDFSSSKR
HHHHHHHHHCCCCCC
58.9522902405
308UbiquitinationQEVTRSLKDFSSSKR
HHHHHHHHHCCCCCC
58.95-
313PhosphorylationSLKDFSSSKRMNTGE
HHHHCCCCCCCCCCC
24.0816997485
321UbiquitinationKRMNTGEKTTMRDLS
CCCCCCCCCCHHHHH
51.11-
328PhosphorylationKTTMRDLSQMLKKMP
CCCHHHHHHHHHHCH
20.1728432305
332AcetylationRDLSQMLKKMPQYQK
HHHHHHHHHCHHHHH
41.5022902405
339AcetylationKKMPQYQKELSKYST
HHCHHHHHHHHHHHH
56.5422902405
364UbiquitinationHYQGTVDKLCRVEQD
HCCCHHHHHHHHHHH
45.19-
382AcetylationGTDAEGEKIKDPMRA
CCCCCCCCCCCHHHH
66.9522902405
384AcetylationDAEGEKIKDPMRAIV
CCCCCCCCCHHHHHH
67.8422902405
411PhosphorylationKIRIILLYIFLKNGI
HHHHHHHHHHHHCCC
6.03-
452PhosphorylationHLGVPIVTDSTLRRR
HHCCCEECHHHHHHC
25.5925403869
454PhosphorylationGVPIVTDSTLRRRSK
CCCEECHHHHHHCCC
21.7025403869
455PhosphorylationVPIVTDSTLRRRSKP
CCEECHHHHHHCCCH
27.3925403869
473PhosphorylationERISEQTYQLSRWTP
HHHHHHHHHHHCCCH
13.7222276854
476PhosphorylationSEQTYQLSRWTPIIK
HHHHHHHHCCCHHHH
15.3922673903
483UbiquitinationSRWTPIIKDIMEDTI
HCCCHHHHHHHHHHH
41.75-
493AcetylationMEDTIEDKLDTKHYP
HHHHHHHCCCCCCCC
35.1622902405
493UbiquitinationMEDTIEDKLDTKHYP
HHHHHHHCCCCCCCC
35.16-
497AcetylationIEDKLDTKHYPYIST
HHHCCCCCCCCCEEE
40.5922902405
497UbiquitinationIEDKLDTKHYPYIST
HHHCCCCCCCCCEEE
40.59-
499PhosphorylationDKLDTKHYPYISTRS
HCCCCCCCCCEEECC
10.1726022182
501PhosphorylationLDTKHYPYISTRSSA
CCCCCCCCEEECCCC
10.5926022182
506PhosphorylationYPYISTRSSASFSTT
CCCEEECCCCCCCCC
30.2825403869
507PhosphorylationPYISTRSSASFSTTA
CCEEECCCCCCCCCC
25.3330411139
509PhosphorylationISTRSSASFSTTAVS
EEECCCCCCCCCCCH
22.9825403869
511PhosphorylationTRSSASFSTTAVSAR
ECCCCCCCCCCCHHC
23.5028432305
512PhosphorylationRSSASFSTTAVSARY
CCCCCCCCCCCHHCC
19.4326022182
513PhosphorylationSSASFSTTAVSARYG
CCCCCCCCCCHHCCC
24.7028432305
516PhosphorylationSFSTTAVSARYGHWH
CCCCCCCHHCCCCCC
12.4528432305
531PhosphorylationKNKAPGEYRSGPRLI
CCCCCCCCCCCCEEE
18.9225403869
533PhosphorylationKAPGEYRSGPRLIIF
CCCCCCCCCCEEEEE
52.8525403869
574PhosphorylationIGSTHILTPQKLLDT
EECCEECCHHHHHHH
24.0715489225
581PhosphorylationTPQKLLDTLKKLNKT
CHHHHHHHHHHHCCC
40.2125403869
583AcetylationQKLLDTLKKLNKTDE
HHHHHHHHHHCCCHH
58.2522902405
590 (in isoform 2)Phosphorylation-63.5628432305
591 (in isoform 2)Phosphorylation-51.4828432305
593PhosphorylationNKTDEEISS------
CCCHHHHCC------
33.0230240740
594PhosphorylationKTDEEISS-------
CCHHHHCC-------
50.3230240740
594 (in isoform 2)Phosphorylation-50.3225403869

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
158SPhosphorylationKinaseCDK5Q03114
GPS
306SPhosphorylationKinasePKCAP04409
PSP
306SPhosphorylationKinasePRKCAP17252
GPS
306SPhosphorylationKinasePKCAP05696
PSP
313SPhosphorylationKinasePKCAP04409
PSP
313SPhosphorylationKinasePRKCAP17252
GPS
313SPhosphorylationKinasePKCAP05696
PSP
574TPhosphorylationKinaseCDK5Q03114
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STXB1_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of STXB1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STX1A_RATStx1aphysical
7768895
STX3_RATStx3physical
7768895
STX2_RATStx2physical
7768895

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STXB1_RAT

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Related Literatures of Post-Translational Modification

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